位置:首页 > 蛋白库 > UBC4_CANAX
UBC4_CANAX
ID   UBC4_CANAX              Reviewed;         147 AA.
AC   P43102;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 4;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 4;
DE   AltName: Full=Ubiquitin carrier protein 4;
DE   AltName: Full=Ubiquitin-protein ligase 4;
GN   Name=UBC4;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7698660; DOI=10.1016/0378-1119(94)00926-j;
RA   Damagnez V., Rolfe M., Cottarel G.;
RT   "Schizosaccharomyces pombe and Candida albicans cDNA homologues of the
RT   Saccharomyces cerevisiae UBC4 gene.";
RL   Gene 155:137-138(1995).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. Mediates the selective degradation of short-lived and
CC       abnormal proteins. Mediates ubiquitination of PEX5.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC         [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC         activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC         conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC         ProRule:PRU10133};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L37383; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P43102; -.
DR   SMR; P43102; -.
DR   VEuPathDB; FungiDB:CAWG_02261; -.
DR   VEuPathDB; FungiDB:CR_09970W_A; -.
DR   UniPathway; UPA00143; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0070628; F:proteasome binding; IEA:EnsemblFungi.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF00179; UQ_con; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..147
FT                   /note="Ubiquitin-conjugating enzyme E2 4"
FT                   /id="PRO_0000082544"
FT   DOMAIN          1..147
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        85
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   147 AA;  16340 MW;  A86557BE37375EB9 CRC64;
     MSLKRINKEL SDLGRDPPSS CSAGPVGDDL YHWQASIMGP PDSPYAGGVF FLSIHFPTDY
     PLKPPKIALT TKIYHPNINS NGNICLDILK DQWSPALTIS KVLLSICSLL TDANPDDPLV
     PEIAHIYKQD RKKYEATAKE WTKKYAV
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024